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方案
98%
旋光性
[α]25/D −7°, c = 0.5 in 1 M HCl
反应适用性
reaction type: solution phase peptide synthesis
mp
259-261 °C (dec.) (lit.)
应用
peptide synthesis
储存温度
2-8°C
SMILES字符串
COc1ccc(C[C@H](N)C(O)=O)cc1
InChI
1S/C10H13NO3/c1-14-8-4-2-7(3-5-8)6-9(11)10(12)13/h2-5,9H,6,11H2,1H3,(H,12,13)/t9-/m0/s1
InChI key
GEYBMYRBIABFTA-VIFPVBQESA-N
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储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
从最新的版本中选择一种：
分析证书(COA)
Lot/Batch Number
Debbie Dewaele et al.
Rapid communications in mass spectrometry : RCM, 30(6), 719-730 (2016-02-13)
Melphalan is a frequently used chemotherapeutical agent for the treatment of myeloma, breast cancer, ovarian cancer and sarcoma of soft tissue. A good knowledge of the reactivity of the drug toward the different amino acids, e.g. covalent adduct formation, is
Ma Diarey Tianero et al.
Nature microbiology, 4(7), 1149-1159 (2019-04-03)
Marine sponges often house small-molecule-producing symbionts extracellularly in their mesohyl, providing the host with a means of chemical defence against predation and microbial infection. Here, we report an intriguing case of chemically mediated symbiosis between the renieramycin-containing sponge Haliclona sp.
Jeffrey K Takimoto et al.
ACS chemical biology, 6(7), 733-743 (2011-05-07)
Unnatural amino acids (Uaas) can be translationally incorporated into proteins in vivo using evolved tRNA/aminoacyl-tRNA synthetase (RS) pairs, affording chemistries inaccessible when restricted to the 20 natural amino acids. To date, most evolved RSs aminoacylate Uaas chemically similar to the
C Lee et al.
Biochemistry and molecular biology international, 31(5), 797-805 (1993-12-01)
An enzyme fraction with catalytic activities for the biosynthesis of the pipecolic acid containing cyclopeptolide SDZ 90-215 was partially purified and characterized from the genus Septoria. The crude cell homogenate was subjected to polyethyleneimine precipitation, ammonium sulfate precipitation and FPLC
Ning Wu et al.
Journal of the American Chemical Society, 126(44), 14306-14307 (2004-11-04)
We have developed a second orthogonal tRNA/synthetase pair for use in yeast based on the Escherichia coli tRNALeu/leucyl tRNA-synthetase pair. Using a novel genetic selection, we have identified a series of synthetase mutants that selectively charge the amber suppresor tRNA
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